ID A0A087QN02_APTFO Unreviewed; 353 AA.
AC A0A087QN02;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Protein AMBP {ECO:0000256|ARBA:ARBA00018905};
GN ORFNames=AS27_11296 {ECO:0000313|EMBL:KFM02606.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02606.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM02606.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02606.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the calycin
CC superfamily. Lipocalin family. {ECO:0000256|ARBA:ARBA00008238}.
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DR EMBL; KL225748; KFM02606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QN02; -.
DR STRING; 9233.A0A087QN02; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd22596; Kunitz_bikunin_1-like; 1.
DR CDD; cd22597; Kunitz_bikunin_2-like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR InterPro; IPR002968; A1-microglobln.
DR InterPro; IPR029856; AMBP.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR46676; PROTEIN AMBP; 1.
DR PANTHER; PTHR46676:SF1; PROTEIN AMBP; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01215; A1MCGLOBULIN.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR00179; LIPOCALIN.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..353
FT /note="Protein AMBP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001828218"
FT DOMAIN 231..281
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 287..337
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 353 AA; 39272 MW; E396980DB49C4DCB CRC64;
MFWGLLSLLL LTMASGTPVR DQDEDIQVQE NFEAERMYGK WYDVAIGTTC KWMKNYKEKF
SMGTLVLGPG PSADQISTAS TRLRQGDCTH ISGAYQKTST PGKYTYYNPK WDVSIRSYVL
RTNYEEYAVI LMKKKSSFGP STTLKLYGRS PELREDLIEA FQQLALEMGI PADSIFILTN
RGECIPQETA TAPLLCASFP VQRARRAVLP PEEGSAVGPL PPYIGNKEDS CRLSRDPGPC
SGMLSRFFYN SSSMACETFL YGGCLGNGNN FYSEKECLQA CRSEAACRLP IVQGPCQKSV
TRWAFDAAQG KCITFSYGGC KGNGNQFYLE KECKEYCGAP PLAEDEEFLH LSN
//
